Abstract:
:Biocatalytic peptide synthesis will benefit from enzymes that are active at low water levels in organic solvent compositions that allow good substrate and product solubility. To explore the use of proteases from thermophiles for peptide synthesis under such conditions, putative protease genes of the subtilase class were cloned from Thermus aquaticus and Deinococcus geothermalis and expressed in Escherichia coli. The purified enzymes were highly thermostable and catalyzed efficient peptide bond synthesis at 80°C and 60°C in neat acetonitrile with excellent conversion (>90%). The enzymes tolerated high levels of N,N-dimethylformamide (DMF) as a cosolvent (40-50% v/v), which improved substrate solubility and gave good conversion in 5+3 peptide condensation reactions. The results suggest that proteases from thermophiles can be used for peptide synthesis under harsh reaction conditions.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Toplak A,Nuijens T,Quaedflieg PJ,Wu B,Janssen DBdoi
10.1016/j.enzmictec.2015.03.003subject
Has Abstractpub_date
2015-06-01 00:00:00pages
20-8eissn
0141-0229issn
1879-0909pii
S0141-0229(15)00047-2journal_volume
73-74pub_type
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journal_title:Enzyme and microbial technology
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